Topic
Aldehyde dehydrogenase
About: Aldehyde dehydrogenase is a research topic. Over the lifetime, 3365 publications have been published within this topic receiving 107683 citations.
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TL;DR: Assessment of the influence of ALDH1A1 on the function and maintenance of the DAergic system in young adult animals with deletion of the Aldh1a1 gene suggests there is altered DA metabolism and dysfunction of theDA transporter and DA release mechanisms.
54 citations
TL;DR: The results indicated that only the ADH-3 isoenzyme effectively oxidized the glycolethers in rat liver, suggesting that the activity of ADH is higher in female than in male rat liver.
54 citations
TL;DR: Unexpectedly, positions with residues unique to one of the four enzymes are about twice as common in both of the horse proteins than in either of the human proteins, showing that not only functional properties of the protein, but also other factors, such as generation time, are important for enzyme divergence.
Abstract: The primary structure of the mitochondrial form of horse liver aldehyde dehydrogenase has been determined, utilizing peptide analyses and homology with other enzyme forms. The subunit exhibits N-terminal heterogeneity in size similar to that for the corresponding human mitochondrial protein, the longest form having 500 residues. Catalase was identified as a contaminant of the preparations. All four pairs within a set of aldehyde dehydrogenases can now be compared, including the same two species variants (horse and human) for both the cytosolic and mitochondrial enzyme, revealing characteristic differences although Cys-302 and other segments of presumed functional importance are unchanged. The cytosolic and mitochondrial enzymes are clearly different (172 exchanges in the horse pair; 160 exchanges in the human pair) and the mitochondrial forms are more conserved (28 exchanges of 500 residues) than the cytosolic ones (43 exchanges). Distributions of the residue substitutions also differ between the two enzyme types. These results suggest a comparatively distant separation of the cytosolic and mitochondrial enzymes into forms with separate functional constraints that are more strict on the mitochondrial than the cytosolic enzyme. Unexpectedly, positions with residues unique to one of the four enzymes are about twice as common in both of the horse proteins than in either of the human proteins. This difference may reflect a general pattern for human/non-human proteins, showing that not only functional properties of the protein, but also other factors, such as generation time (longer in man than in horse), are important for enzyme divergence.
54 citations
TL;DR: It is shown that alcohol consumption itself depresses hepatic aldehyde dehydrogenase activity, and it is unlikely that the low hepaticAldehyde dehydration activity reported in alcoholics represents a primary abnormality predisposing to alcoholism or alcoholic liver disease.
54 citations